GSBS Student Publications
Title
Actin-related proteins (Arps): conformational switches for chromatin-remodeling machines
GSBS Program
Biochemistry & Molecular Pharmacology
UMMS Affiliation
Graduate School of Biomedical Sciences; Program in Molecular Medicine
Date
7-6-2000
Document Type
Article
Medical Subject Headings
Actins; Adenosine Triphosphatases; Amino Acid Sequence; Animals; Chromatin; Models, Biological; Models, Molecular; Protein Conformation
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
The actin superfamily of ATPases includes cytoskeletal actins, the stress 70 proteins (e.g. hsc70), sugar kinases, glycerol kinase, and several prokaryotic cell cycle proteins. Although these proteins share limited sequence identity, they all appear to maintain a similar tertiary structure, the "actin fold", which may serve to couple ATP hydrolysis to protein conformational changes. Recently, an actin-related protein (Arp) subfamily has been identified based on sequence homology to conventional actin. Although some Arps are clearly involved in cytoskeletal functions, both actin and/or Arps have been found as stoichiometric subunits of several nuclear chromatin-remodeling enzymes. Here we present two related models in which actin and/or Arps function as conformational switches that control either the activity or the assembly of chromatin-remodeling machines.
Rights and Permissions
Citation: Bioessays. 2000 Jul;22(7):666-72. Link to article on publisher's site
DOI of Published Version
10.1002/1521-1878(200007)22:7.3.0.CO;2-Y
Related Resources
Journal Title
BioEssays : news and reviews in molecular, cellular and developmental biology
PubMed ID
10878579
Repository Citation
Boyer, Laurie A. and Peterson, Craig L., "Actin-related proteins (Arps): conformational switches for chromatin-remodeling machines" (2000). GSBS Student Publications. 120.
https://escholarship.umassmed.edu/gsbs_sp/120